7dfv
From Proteopedia
(Difference between revisions)
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<StructureSection load='7dfv' size='340' side='right'caption='[[7dfv]], [[Resolution|resolution]] 2.99Å' scene=''> | <StructureSection load='7dfv' size='340' side='right'caption='[[7dfv]], [[Resolution|resolution]] 2.99Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DFV FirstGlance]. <br> |
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.99Å</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.99Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7dfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dfv OCA], [https://pdbe.org/7dfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dfv RCSB], [https://www.ebi.ac.uk/pdbsum/7dfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dfv ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7dfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dfv OCA], [https://pdbe.org/7dfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dfv RCSB], [https://www.ebi.ac.uk/pdbsum/7dfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dfv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
- | == | + | <div style="background-color:#fffaf0;"> |
- | + | == Publication Abstract from PubMed == | |
+ | Direct or indirect recognition of pathogen-derived effectors by plant nucleotide-binding leucine-rich repeat (LRR) receptors (NLRs) initiates innate immune responses. The Hyaloperonospora arabidopsidis effector ATR1 activates the N-terminal Toll-interleukin-1 receptor (TIR) domain of Arabidopsis NLR RPP1. We report a cryo-electron microscopy structure of RPP1 bound by ATR1. The structure reveals a C-terminal jelly roll/Ig-like domain (C-JID) for specific ATR1 recognition. Biochemical and functional analyses show that ATR1 binds to the C-JID and the LRRs to induce an RPP1 tetrameric assembly required for nicotinamide adenine dinucleotide hydrolase (NADase) activity. RPP1 tetramerization creates two potential active sites, each formed by an asymmetric TIR homodimer. Our data define the mechanism of direct effector recognition by a plant NLR leading to formation of a signaling-active holoenzyme. | ||
+ | |||
+ | Direct pathogen-induced assembly of an NLR immune receptor complex to form a holoenzyme.,Ma S, Lapin D, Liu L, Sun Y, Song W, Zhang X, Logemann E, Yu D, Wang J, Jirschitzka J, Han Z, Schulze-Lefert P, Parker JE, Chai J Science. 2020 Dec 4;370(6521). pii: 370/6521/eabe3069. doi:, 10.1126/science.abe3069. PMID:33273071<ref>PMID:33273071</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 7dfv" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Arabidopsis thaliana]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chai JJ]] | [[Category: Chai JJ]] |
Current revision
Cryo-EM structure of plant NLR RPP1 tetramer core part
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Categories: Large Structures | Chai JJ | Han ZF | Jirschitzka J | Lapin D | Liu L | Logemann E | Ma SC | Parker JE | SchulzeLefert P | Song W | Sun Y | Wang J | Yu DL | Zhang XX